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Database: PDB
Entry: 2KYH
LinkDB: 2KYH
Original site: 2KYH 
HEADER    MEMBRANE PROTEIN                        26-MAY-10   2KYH              
TITLE     SOLUTION STRUCTURE OF THE VOLTAGE-SENSING DOMAIN OF KVAP              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: VOLTAGE-GATED POTASSIUM CHANNEL;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 18-160;                                       
COMPND   5 SYNONYM: KVAP;                                                       
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: AEROPYRUM PERNIX;                               
SOURCE   3 ORGANISM_TAXID: 56636;                                               
SOURCE   4 GENE: APE_0955;                                                      
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PQE60                                     
KEYWDS    ION CHANNEL, MEMBRANE PROTEIN                                         
EXPDTA    SOLUTION NMR                                                          
NUMMDL    20                                                                    
AUTHOR    J.A.BUTTERWICK,R.MACKINNON                                            
REVDAT   3   03-NOV-10 2KYH    1       JRNL                                     
REVDAT   2   06-OCT-10 2KYH    1       JRNL   REMARK                            
REVDAT   1   29-SEP-10 2KYH    0                                                
JRNL        AUTH   J.A.BUTTERWICK,R.MACKINNON                                   
JRNL        TITL   SOLUTION STRUCTURE AND PHOSPHOLIPID INTERACTIONS OF THE      
JRNL        TITL 2 ISOLATED VOLTAGE-SENSOR DOMAIN FROM KVAP.                    
JRNL        REF    J.MOL.BIOL.                   V. 403   591 2010              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   20851706                                                     
JRNL        DOI    10.1016/J.JMB.2010.09.012                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR_NIH                                           
REMARK   3   AUTHORS     : SCHWIETERS, KUSZEWSKI, TJ                            
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2KYH COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAY-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB101731.                                      
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 318                                
REMARK 210  PH                             : 7.0                                
REMARK 210  IONIC STRENGTH                 : 40                                 
REMARK 210  PRESSURE                       : AMBIENT                            
REMARK 210  SAMPLE CONTENTS                : 0.1-0.5 MM [U-98% 15N] ENTITY,     
REMARK 210                                   20 MM HEPES, 20 MM POTASSIUM       
REMARK 210                                   CHLORIDE, >5 MM DIHEPTANOYL        
REMARK 210                                   PHOSPHATIDYLCHOLINE, 90% H2O/10%   
REMARK 210                                   D2O; 0.1-0.5 MM [U-100% 13C; U-    
REMARK 210                                   100% 15N; U-80% 2H] ENTITY, 20 MM  
REMARK 210                                   HEPES, 20 MM POTASSIUM CHLORIDE,   
REMARK 210                                   >5 MM DIHEPTANOYL                  
REMARK 210                                   PHOSPHATIDYLCHOLINE, 90% H2O/10%   
REMARK 210                                   D2O; 0.1-0.5 MM [U-98% 13C; U-98%  
REMARK 210                                   15N] ENTITY, 20 MM HEPES, 20 MM    
REMARK 210                                   POTASSIUM CHLORIDE, >5 MM          
REMARK 210                                   DIHEPTANOYL PHOSPHATIDYLCHOLINE,   
REMARK 210                                   90% H2O/10% D2O; 0.1-0.5 MM        
REMARK 210                                   [13CH3/12CD2]-LEU,VAL,[13CH3]-ILE  
REMARK 210                                   ENTITY, 20 MM HEPES, 20 MM         
REMARK 210                                   POTASSIUM CHLORIDE, >5 MM          
REMARK 210                                   DIHEPTANOYL PHOSPHATIDYLCHOLINE,   
REMARK 210                                   90% H2O/10% D2O                    
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 2D 1H-15N HSQC; 3D HNCO; 3D        
REMARK 210                                   HNCA; 3D HN(CO)CA; 3D HCCH-COSY;   
REMARK 210                                   3D HN(CO)CACB; 3D 1H-15N NOESY;    
REMARK 210                                   3D 1H-13C NOESY                    
REMARK 210  SPECTROMETER FIELD STRENGTH    : 900 MHZ; 800 MHZ; 700 MHZ; 600     
REMARK 210                                   MHZ                                
REMARK 210  SPECTROMETER MODEL             : DMX                                
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : NMRPIPE, SPARKY                    
REMARK 210   METHOD USED                   : SIMULATED ANNEALING                
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 100                                
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 20                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH THE LOWEST ENERGY  
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 210                                                                      
REMARK 210 REMARK: LOWEST ENERGY STRUCTURE IS MODEL 1. STRUCTURE CLOSEST TO     
REMARK 210  THE MEAN COORDINATES IS MODEL 20.                                   
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   HG   SER A    80     H    ASP A    82              1.25            
REMARK 500   O    THR A    90     H    GLU A    93              1.58            
REMARK 500   O    TRP A    70     H    ALA A    74              1.59            
REMARK 500   O    ALA A   144     H    LEU A   148              1.60            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500  1 ARG A   6      116.28     56.72                                   
REMARK 500  1 GLU A  23       28.52    -74.40                                   
REMARK 500  1 PRO A  25      -39.75    -39.49                                   
REMARK 500  1 GLN A  49       57.86   -117.37                                   
REMARK 500  1 LEU A  50      165.31    -42.21                                   
REMARK 500  1 VAL A  98       94.96    -32.01                                   
REMARK 500  1 VAL A 149       74.48     16.64                                   
REMARK 500  2 SER A   9       52.58   -102.24                                   
REMARK 500  2 LEU A  11       67.03   -105.85                                   
REMARK 500  2 MET A  22       -2.79    -57.32                                   
REMARK 500  2 GLN A  49       56.08   -112.89                                   
REMARK 500  2 LEU A  50      165.48    -45.68                                   
REMARK 500  2 ASP A  82       83.80   -152.19                                   
REMARK 500  2 THR A  90       31.57    -95.90                                   
REMARK 500  2 VAL A 149       70.49     58.46                                   
REMARK 500  3 SER A   9       48.17    -74.19                                   
REMARK 500  3 GLN A  49       52.89     32.79                                   
REMARK 500  3 LEU A  50      176.05    -46.24                                   
REMARK 500  3 ASP A  82       80.12   -151.59                                   
REMARK 500  3 VAL A 149       73.13     26.88                                   
REMARK 500  4 ARG A   6      -65.39     63.68                                   
REMARK 500  4 ASP A  10     -142.07    -69.01                                   
REMARK 500  4 LEU A  11      -36.50     68.34                                   
REMARK 500  4 VAL A  98      106.80    -39.01                                   
REMARK 500  4 PRO A 150      -70.20    -74.87                                   
REMARK 500  5 SER A   9      169.79     51.11                                   
REMARK 500  5 LEU A  11       71.45   -172.20                                   
REMARK 500  5 ARG A  14      -68.30   -167.18                                   
REMARK 500  5 HIS A  24      151.51    -44.90                                   
REMARK 500  5 PRO A  25      -39.80    -39.41                                   
REMARK 500  5 GLN A  49       67.93   -103.25                                   
REMARK 500  5 LEU A  50      157.49    -38.38                                   
REMARK 500  5 ASP A  82       82.34   -150.63                                   
REMARK 500  5 VAL A  98      100.81    -35.59                                   
REMARK 500  5 PHE A 137      -70.87    -59.76                                   
REMARK 500  6 LEU A   8      156.88     58.46                                   
REMARK 500  6 PRO A  25      -35.33    -39.22                                   
REMARK 500  6 GLN A  49       61.74   -114.26                                   
REMARK 500  6 LEU A  50      172.19    -46.31                                   
REMARK 500  6 ASP A  82       70.95   -153.54                                   
REMARK 500  7 LEU A   8       92.96     54.36                                   
REMARK 500  7 SER A   9      -40.38   -164.80                                   
REMARK 500  7 LEU A  11      -90.79   -103.01                                   
REMARK 500  7 GLN A  49       64.60   -108.29                                   
REMARK 500  7 LEU A  50      164.42    -44.83                                   
REMARK 500  7 LEU A  97       40.18   -102.71                                   
REMARK 500  7 VAL A 149       78.83     19.49                                   
REMARK 500  8 LEU A  11     -109.05    -82.75                                   
REMARK 500  8 VAL A  15      -63.98   -147.43                                   
REMARK 500  8 GLN A  49       61.08   -107.15                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     145 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 16957   RELATED DB: BMRB                                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 PROCESSING BY THE E. COLI HOST HAS CHANGED THE FIRST FIVE RESIDUES   
REMARK 999 (MET ALA ARG PHE ARG) TO LEU.                                        
DBREF  2KYH A    5   147  UNP    Q9YDF8   KVAP_AERPE      18    160             
SEQADV 2KYH LEU A    5  UNP  Q9YDF8    ARG    18 SEE REMARK 999                 
SEQADV 2KYH LEU A  148  UNP  Q9YDF8              EXPRESSION TAG                 
SEQADV 2KYH VAL A  149  UNP  Q9YDF8              EXPRESSION TAG                 
SEQADV 2KYH PRO A  150  UNP  Q9YDF8              EXPRESSION TAG                 
SEQADV 2KYH ARG A  151  UNP  Q9YDF8              EXPRESSION TAG                 
SEQRES   1 A  147  LEU ARG GLY LEU SER ASP LEU GLY GLY ARG VAL ARG ASN          
SEQRES   2 A  147  ILE GLY ASP VAL MET GLU HIS PRO LEU VAL GLU LEU GLY          
SEQRES   3 A  147  VAL SER TYR ALA ALA LEU LEU SER VAL ILE VAL VAL VAL          
SEQRES   4 A  147  VAL GLU TYR THR MET GLN LEU SER GLY GLU TYR LEU VAL          
SEQRES   5 A  147  ARG LEU TYR LEU VAL ASP LEU ILE LEU VAL ILE ILE LEU          
SEQRES   6 A  147  TRP ALA ASP TYR ALA TYR ARG ALA TYR LYS SER GLY ASP          
SEQRES   7 A  147  PRO ALA GLY TYR VAL LYS LYS THR LEU TYR GLU ILE PRO          
SEQRES   8 A  147  ALA LEU VAL PRO ALA GLY LEU LEU ALA LEU ILE GLU GLY          
SEQRES   9 A  147  HIS LEU ALA GLY LEU GLY LEU PHE ARG LEU VAL ARG LEU          
SEQRES  10 A  147  LEU ARG PHE LEU ARG ILE LEU LEU ILE ILE SER ARG GLY          
SEQRES  11 A  147  SER LYS PHE LEU SER ALA ILE ALA ASP ALA ALA ASP LYS          
SEQRES  12 A  147  LEU VAL PRO ARG                                              
HELIX    1   1 GLY A   13  MET A   22  1                                  10    
HELIX    2   2 HIS A   24  MET A   48  1                                  25    
HELIX    3   3 SER A   51  SER A   80  1                                  30    
HELIX    4   4 ASP A   82  THR A   90  1                                   9    
HELIX    5   5 GLU A   93  VAL A   98  1                                   6    
HELIX    6   6 PRO A   99  LEU A  113  1                                  15    
HELIX    7   7 LEU A  115  VAL A  149  1                                  35    
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
MODEL        1                                                                  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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